Biochemical characterization of laboratory mutants of extended-spectrum β-lactamase TEM-60

Bibiana Caporale, Nicola Franceschini, Mariagrazia Perilli, Bernardetta Segatore, Gian Maria Rossolini, Gianfranco Amicosante

Research output: Contribution to journalArticle

Abstract

Three mutants of the extended-spectrum β-lactamase TEM-60, the P51L, K104E, and S164R mutants, were constructed by site-directed mutagenesis. The kinetic parameters of the mutated enzymes and interactions of inhibitors were significantly different from those of TEM-60, revealing that the L51P mutation plays an important role in enzyme activity and stability in the TEM-60 background.

Original languageEnglish
Pages (from-to)3579-3582
Number of pages4
JournalAntimicrobial Agents and Chemotherapy
Volume48
Issue number9
DOIs
Publication statusPublished - Sep 2004

ASJC Scopus subject areas

  • Pharmacology (medical)

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    Caporale, B., Franceschini, N., Perilli, M., Segatore, B., Rossolini, G. M., & Amicosante, G. (2004). Biochemical characterization of laboratory mutants of extended-spectrum β-lactamase TEM-60. Antimicrobial Agents and Chemotherapy, 48(9), 3579-3582. https://doi.org/10.1128/AAC.48.9.3579-3582.2004